http://purl.uniprot.org/citations/18390652 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/18390652 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/18390652 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
http://purl.uniprot.org/citations/18390652 | http://www.w3.org/2000/01/rdf-schema#comment | "YgaF, a protein of previously unknown function in Escherichia coli, was shown to possess noncovalently bound flavin adenine dinucleotide and to exhibit L-2-hydroxyglutarate oxidase activity. The inability of anaerobic, reduced enzyme to reverse the reaction by reducing the product alpha-ketoglutaric acid is explained by the very high reduction potential (+19 mV) of the bound cofactor. The likely role of this enzyme in the cell is to recover alpha-ketoglutarate mistakenly reduced by other enzymes or formed during growth on propionate. On the basis of the identified function, we propose that this gene be renamed lhgO."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.01977-07"xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.01977-07"xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/author | "Hausinger R.P."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/author | "Hausinger R.P."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/author | "Mulrooney S.B."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/author | "Mulrooney S.B."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/author | "Kalliri E."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/author | "Kalliri E."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/pages | "3793-3798"xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/pages | "3793-3798"xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/title | "Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/title | "Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase."xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/volume | "190"xsd:string |
http://purl.uniprot.org/citations/18390652 | http://purl.uniprot.org/core/volume | "190"xsd:string |
http://purl.uniprot.org/citations/18390652 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18390652 |
http://purl.uniprot.org/citations/18390652 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18390652 |
http://purl.uniprot.org/citations/18390652 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18390652 |